ID CP21C_ARATH Reviewed; 230 AA. AC Q94A16; C0Z333; O22906; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 2. DT 09-JUL-2014, entry version 88. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP21-3, mitochondrial; DE Short=PPIase CYP21-3; DE EC=5.2.1.8; DE AltName: Full=Cyclophilin of 21 kDa 3; DE AltName: Full=Rotamase CYP21-3; DE Flags: Precursor; GN Name=CYP21-3; OrderedLocusNames=At2g47320; ORFNames=T8I13.16; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, GENE RP FAMILY, AND NOMENCLATURE. RX PubMed=15051864; DOI=10.1104/pp.103.022160; RA Romano P.G.N., Horton P., Gray J.E.; RT "The Arabidopsis cyclophilin gene family."; RL Plant Physiol. 134:1268-1282(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=cv. Columbia; TISSUE=Rosette leaf; RX PubMed=19423640; DOI=10.1093/dnares/dsp009; RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., RA Seki M., Shinozaki K.; RT "Analysis of multiple occurrences of alternative splicing events in RT Arabidopsis thaliana using novel sequenced full-length cDNAs."; RL DNA Res. 16:155-164(2009). RN [6] RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE. RX PubMed=15047905; DOI=10.1104/pp.103.031005; RA He Z., Li L., Luan S.; RT "Immunophilins and parvulins. Superfamily of peptidyl prolyl RT isomerases in Arabidopsis."; RL Plant Physiol. 134:1248-1267(2004). RN [7] RP INDUCTION. RX PubMed=16173598; DOI=10.1021/es050385r; RA Ekman D.R., Wolfe N.L., Dean J.F.D.; RT "Gene expression changes in Arabidopsis thaliana seedling roots RT exposed to the munition hexahydro-1,3,5-trinitro-1,3,5-triazine."; RL Environ. Sci. Technol. 39:6313-6320(2005). CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- ENZYME REGULATION: Binds cyclosporin A (CsA). CsA mediates some of CC its effects via an inhibitory action on PPIase (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q94A16-1; Sequence=Displayed; CC Name=2; CC IsoId=Q94A16-2; Sequence=VSP_055389; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Ubiquitous, mostly in aerial organs. CC -!- INDUCTION: Repressed by the munition hexahydro-1,3,5-trinitro- CC 1,3,5-triazine, also known as Royal Demolition eXplosive (RDX). CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAK91465.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=AAK91465.1; Type=Erroneous termination; Positions=82; Note=Translated as Leu; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY568520; AAS75303.1; -; mRNA. DR EMBL; AC002337; AAB63832.1; -; Genomic_DNA. DR EMBL; CP002685; AEC10827.1; -; Genomic_DNA. DR EMBL; AY050450; AAK91465.1; ALT_INIT; mRNA. DR EMBL; AY097351; AAM19867.1; -; mRNA. DR EMBL; AK318997; BAH57112.1; -; mRNA. DR PIR; G84913; G84913. DR RefSeq; NP_182254.1; NM_130300.3. DR UniGene; At.12226; -. DR UniGene; At.25582; -. DR ProteinModelPortal; Q94A16; -. DR SMR; Q94A16; 87-223. DR PaxDb; Q94A16; -. DR PRIDE; Q94A16; -. DR EnsemblPlants; AT2G47320.1; AT2G47320.1; AT2G47320. DR GeneID; 819345; -. DR KEGG; ath:AT2G47320; -. DR TAIR; AT2G47320; -. DR eggNOG; COG0652; -. DR HOGENOM; HOG000006244; -. DR OMA; SRISITN; -. DR PhylomeDB; Q94A16; -. DR BioCyc; ARA:AT2G47320-MONOMER; -. DR Genevestigator; Q94A16; -. DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0042277; F:peptide binding; IEA:UniProtKB-KW. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW. DR Gene3D; 2.40.100.10; -; 1. DR InterPro; IPR029000; Cyclophilin-like_dom. DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR SUPFAM; SSF50891; SSF50891; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Chaperone; Complete proteome; Cyclosporin; KW Isomerase; Mitochondrion; Reference proteome; Rotamase; KW Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 230 Peptidyl-prolyl cis-trans isomerase FT CYP21-3, mitochondrial. FT /FTId=PRO_0000044628. FT DOMAIN 76 226 PPIase cyclophilin-type. FT VAR_SEQ 1 70 Missing (in isoform 2). FT /FTId=VSP_055389. SQ SEQUENCE 230 AA; 26042 MW; 6198D43EE5B9552F CRC64; MAKIKPQALL QQSKKKKGPS RISITNIVIY TLAVLLLVFV LFSAYRRWTH RSEIPTHNGR SVLEDAAFPG MKNVDLPRFA TLDTGKGSVT IELFKDTAPN VVDQFMKFCQ DGYFKGFLFS RVVKHFVIQA GDSAEFDAVK DWALDRKNID TSLKHEEFMV GTPKAKNEQG GFEFFIVSAQ IKDLNEKLTV FGRVSKGQDV VQEIEEVETD DQYQPKSPIE IMSVTLLQDM //